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  Ribosome dynamics during decoding.

Rodnina, M. V., Fischer, N., Maracci, C., & Stark, H. (2017). Ribosome dynamics during decoding. Philosophical Transactions of the Royal Society B, 372(1716): 20160182. doi:10.1098/rstb.2016.0182.

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 Creators:
Rodnina, M. V.1, Author           
Fischer, N.2, Author           
Maracci, C.1, Author           
Stark, H.2, Author           
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1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              
2Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_2205645              

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Free keywords: ribosome, tRNA, translation. decoding, recoding
 Abstract: Elongation factors Tu (EF-Tu) and SelB are translational GTPases that deliver aminoacyl-tRNAs (aa-tRNAs) to the ribosome. In each canonical round of translation elongation, aa-tRNAs, assisted by EF-Tu, decode mRNA codons and insert the respective amino acid into the growing peptide chain. Stop codons usually lead to translation termination; however, in special cases UGA codons are recoded to selenocysteine (Sec) with the help of SelB. Recruitment of EF-Tu and SelB together with their respective aa-tRNAs to the ribosome is a multistep process. In this review, we summarize recent progress in understanding the role of ribosome dynamics in aa-tRNA selection. We describe the path to correct codon recognition by canonical elongator aa-tRNA and Sec-tRNASec and discuss the local and global rearrangements of the ribosome in response to correct and incorrect aa-tRNAs. We present the mechanisms of GTPase activation and GTP hydrolysis of EF-Tu and SelB and summarize what is known about the accommodation of aa-tRNA on the ribosome after its release from the elongation factor. We show how ribosome dynamics ensures high selectivity for the cognate aa-tRNA and suggest that conformational fluctuations, induced fit and kinetic discrimination play major roles in maintaining the speed and fidelity of translation.This article is part of the themed issue 'Perspectives on the ribosome'.

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Language(s): eng - English
 Dates: 2017-01-302017-03-19
 Publication Status: Issued
 Pages: -
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 Rev. Type: Peer
 Identifiers: DOI: 10.1098/rstb.2016.0182
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Title: Philosophical Transactions of the Royal Society B
Source Genre: Journal
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Pages: 10 Volume / Issue: 372 (1716) Sequence Number: 20160182 Start / End Page: - Identifier: -